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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



ID: 318527.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Dual Function of Protein Confinement in Chaperonin-assisted Protein Folding
Authors:Brinker, A.; Pfeifer, G.; Kerner, M. J.; Naylor, D. J.; Hartl, F. U.; Hayer-Hartl, M. K.
Date of Publication (YYYY-MM-DD):2001
Title of Journal:Cell
Volume:107
Issue / Number:2
Start Page:223
End Page:233
Audience:Not Specified
Abstract / Description:The GroEL/GroES chaperonin system mediates the folding of a range of newly synthesized polypeptides in the bacterial cytosol. Using a rapid biotin-streptavidin-based inhibition of chaperonin function, we show that the cage formed by GroEL and its cofactor GroES can have a dual role in promoting folding. First, enclosure of nonnative protein in the GroEL:GroES complex is essential for folding to proceed unimpaired by aggregation. Second, folding inside the cage can be significantly faster than folding in free solution, independently of ATP-driven cycles of GroES binding and release. This suggests that confinement of unfolded protein in the narrow hydrophilic space of the chaperonin cage smoothes the energy landscape for the folding of some proteins, increasing the flux of folding intermediates toward the native state.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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